Analytical Data
-
基因名
HSPA1L
- Application
-
别名
Heat shock 70 kDa protein 1-like; Heat shock 70 kDa protein 1-Hom; HSP70-Hom; Heat shock protein family A member 1L; HSPA1L; Homo sapiens; Human; Heat shock 70 kDa protein 1L
-
种属
Human
-
表达系统
E. coli
-
标签
Strep;His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P34931
-
表达区间
A2-D641
-
蛋白长度
Partial
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
HSPA1L, a member of the heat shock protein 70 (HSP70) family, plays a significant role in cellular stress response, protein folding, and degradation pathways. Its expression is particularly elevated during stressful conditions such as heat shock, oxidative stress, and inflammation, suggesting its protective role in maintaining cellular homeostasis. Research has shown that HSPA1L is involved in various biological processes, including cell proliferation, apoptosis, and differentiation, making it a crucial factor in both normal physiology and disease states. Importantly, HSPA1L has also been implicated in cancer progression, where it can modulate tumor growth and response to therapy. Given its multifunctional role, the recombinant production of HSPA1L protein is of great interest for understanding its mechanisms and for potential therapeutic applications. Studies focusing on the characterization and functional analysis of HSPA1L recombinant protein aim to provide insights into its specific interactions, regulatory pathways, and role in diseases, particularly in oncological contexts. The ability to produce HSPA1L in a recombinant form allows researchers to perform detailed biochemical assays, investigate its chaperone activity, and explore its potential as a biomarker or therapeutic target. As such, HSPA1L represents a promising avenue for research in cellular stress responses, cancer biology, and other related fields.
